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| − | '''15 June 2020:''' ''Continued growth among the esterases.'' The '''[[Carbohydrate Esterase Family 3]]''' page, [[Author]]ed by grad student '''[[User:Stefen Stangherlin|Stefen Stangherlin]]''', was finalized and [[Curator Approved]] by '''[[User:Joel Weadge|Joel Weadge]]''' and '''[[User:Michael Suits|Michael Suits]]''' today. '''[[CE3]]''' comprises a group of specific acetyl-xylan esterases with a rich history of initial discovery, mechanistic analysis, and structural characterization. ''We thank '''[[User:Stefen Stangherlin|Stefen]]''', '''[[User:Joel Weadge|Joel]]''', and '''[[User:Michael Suits|Mike]]''' for contributing yet another page to the growing [[Carbohydrate Esterase Families|CE family section]] in CAZypedia - read more on CE3 '''[[CE3|here]]'''.'' | + | '''2 May 2024:''' ''CBDs I to X... A major milestone!'' '''CBM families 1 to 10 are now complete!''' These are the old CBD (cellulose-binding domain) families, which used to have roman numerals as part of their nomenclature. A special thank you to all the authors and responsible curators who have contributed to this major milestone. Go have a peek at each of these old school families on their respective ''CAZypedia'' pages: '''[[CBM1]], [[CBM2]], [[CBM3]], [[CBM4]], [[CBM5]], [[CBM6]], [[CBM7]], [[CBM8]], [[CBM9]], and [[CBM10]]'''. |
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| − | | + | '''11 February 2024:''' ''A "BLAST" from the past, with a fresh update.'' [[Author]] '''[[User:Eduardo Moreno Prieto|Eduardo Moreno Prieto]]''' composed a new page on '''[[Glycoside Hydrolase Family 119]]''',a family of bacterial amylases, which was [[Curator Approved]] by '''[[User:Stefan Janecek|Stefan Janecek]]''' and '''[[User:Bernard Henrissat|Bernard Henrissat]]''' today. The first member of '''[[GH119]]''' was characterized in 2006, and through sequence analysis with [[GH57]] members, [[User:Stefan Janecek|Janeček]] and Kuchtová predicted the active-site residues in 2012. Over a decade later, '''[[User:Eduardo Moreno Prieto|Eduardo]]''', '''[[User:Bernard Henrissat|Bernard]]''', and colleagues finally provided critical experimental support for these predictions. ''Learn more about this history, and especially the relationship between '''[[GH119]]''' and '''[[GH57]]''', in CAZypedia.'' |
| − | '''15 May 2020:''' ''CBM20 for 2020!'' The multifunctional starch-disrupting, starch-binding and enzyme targeting [[CBM20]] family is now up and running in ''CAZypedia''. These pervasive CBMs have been identified in CAZy families including [[glycoside hydrolases]] and [[Auxiliary Activity Families|lytic polysaccharide monooxygenases]] but also in non-CAZy enzymes. The page was authored by '''[[User:Marie Sofie Moeller|Marie Sofie Møller]]''' with '''[[User:Birte Svensson|Birte Svensson]]''' and '''[[User:Stefan Janecek|Stefan Janecek]]''' acting as responsible curators. ''Find out more on this starch-interacting family '''[[CBM20|here]]'''.'' | |
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| − | '''15 May 2020:''' ''More on beta(1,3)-glucanases.'' The '''[[Glycoside Hydrolase Family 64]]''' page, [[Author]]ed by '''[[User:Julie Grondin|Julie Grondin]]''', was completed and [[Curator Approved]] today. '''[[GH64]]''' comprises a group of β-1,3-glucanases, primarily from bacteria.The archetype of this family was originally cloned from a ''Streptomyces'' species in the late 1990's and was the subject of mechanistic and structural analysis through the first decade of the new millenium. Notably, analysis by a team led by '''[[User:Bernard Henrissat|Bernard Henrissat]]''' defined that this enzyme, and thus family, uses an [[inverting]] mechanism, further disntiguishing it from well-known [[retaining]] beta(1,3)-glucanases of [[GH16]], [[GH17]], and others, including the recently described [[GH158]] beta(1,3)-glucanases reported below. ''Read more about the unique '''[[Glycoside Hydrolase Family 64|Glycoside Hydrolase Family 64 here]]'''.'' | + | '''3 February 2024:''' ''A new family of beta-1,2-glucan-cyclizing enzymes.'' A page on the (currently) newest GH family, '''[[Glycoside Hydrolase Family 189]]''', was completed today by [[Author]]s '''[[User:Tomoko Masaike|Tomoko Masaike]]''', '''[[User:Masahiro Nakajima|Masahiro Nakajima]]''', and '''[[User:Nobukiyo Tanaka|Nobukiyo Tanaka]]''' ([[User:Masahiro Nakajima|Masahiro Nakajima]] is the [[Responsible Curator]]). '''[[GH189]]''' is a family of bacterial transglycosylases that comprise a critical domain in cyclic beta-1,2-glucan synthase (CGS), because this domain is responsible for the final cyclization step during the biosynthesis of these key effector molecules. The discovery of '''[[GH189]]''' builds on similarly exciting work by these authors and their colleagues on beta-1,2-glucan hydrolases in [[GH144]] and [[GH162]], which share a common protein fold with '''[[GH189]]''', but have distinct mechansims. ''Check out the '''[[GH189]]''', [[GH144]], and [[GH162]] pages to learn more about this breakthrough work on beta-1,2-glucan-active enzymes!'' |
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| − | '''11 May 2020:''' ''Three more from the gut.'' '''[[User:Alan Cartmell|Alan Cartmell]]''' completed no less than three new [[Glycoside Hydrolase Families|Glycoside Hydrolase Family]] pages on this day. '''[[Glycoside Hydrolase Family 137]]''', '''[[Glycoside Hydrolase Family 140]]''', and '''[[Glycoside Hydrolase Family 145]]''' were all created from a series of studies of Polysacchardie Utilization Loci from human gut bacteria by '''[[User:Harry Gilbert|Harry Gilbert]]'s''' group, to which '''[[User:Alan Cartmell|Alan]]''' contributed defining crystallography. '''[[User:Alan Cartmell|Alan]]''' has also taken over the duty of [[Responsible Curator]] of these pages following the retirement of the venerable '''[[User:Harry Gilbert|Professor Gilbert]]''', one of ''CAZypedia's'' [[CAZypedia:History|founding Senior Curators]]. ''Read more about the substrate specificity and structural biology of these three diverse families on their corresponding pages.''
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| − | '''6 May 2020:''' ''CE #1!'' The first [[Carbohydrate Esterase Families|Carbohydrate Esterase Family]] page in the series, '''[[CE1]]''', was [[Curator Approved]] today. [[Author]]ed by '''[[User:Casper Wilkens|Casper Wilkens]]''', the '''[[Carbohydrate Esterase Family 1]]''' page describes an old family of carbohydrate-specific and other esterases, members of which were identified through classical biochemistry before the present age of easy gene cloning and sequencing. Carbohydrate-active members of '''[[CE1]]''' include acetyl xylan esterases, cinnamoyl esterases, and feruloyl esterases responsible for hydrolyzing pendant acyl groups from plant cell wall matrix glycans (hemicelluloses). ''Read more about the long history of '''[[Carbohydrate Esterase Family 1]]''' here.''
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| − | '''10 April 2020:''' ''Yet another new one from the gut.'' Today, [[Author]] '''[[User:Kazune Tamura|Kazune Tamura]]''' completed the '''[[Glycoside Hydrolase Family 158]]''' page. '''[[GH158]]''' emerged in 2019 from a high-throughput biochemical survey of sequences identified as distantly related to [[glycoside hydrolases]] by the CAZy team, who first demonstrated ''endo''-beta(1,3)-glucanase activity for the founding member of the family from the human gut bacterium ''Victivallis vadensis''. Contemporaneously, analysis of homolgos from human gut ''Bacteroides'' species by Guillaume Dejean and '''[[User:Kazune Tamura|Kazune Tamura]]''' resolved details of the specificity, mechanism, and tertiary structure of '''[[GH158]]''' members in Polysaccharide Utilization Loci. ''Read about the detailed history and juicy details of this new GH family '''[[Glycoside Hydrolase Family 158|here]]'''.'' | |
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| − | '''8 April 2020:''' ''Another new one from the gut.'' The '''[[Glycoside Hydrolase Family 164]]''' page, which was [[author]]ed by '''[[User:Zachary Armstrong|Zachary Armstrong]]''', was upgraded to [[Curator Approved]] status by [[Responsible Curator]] '''[[User:Gideon Davies|Gideon Davies]]''' today. '''[[Glycoside Hydrolase Family 164]]''' is yet another newly discovered [[Glycoside Hydrolase Families|GH family]] from a human gut bacterium - this time through a large-scale effort by teams at AFMB and CERMAV spearheaded by [[User:Bernard Henrissat|Bernard Henrissat]]. The founding member of '''[[GH164]]''' is a beta-mannosidase from ''Bacteroides salyersiae'', on which '''[[User:Zachary Armstrong|Zach]]''' and '''[[User:Gideon Davies|Gideon]]''' performed a classic mechanistic and structural analysis to define the central aspects of catalysis in this new family. ''Read more about this new - and currently tiny - GH family '''[[Glycoside Hydrolase Family 164|here]]'''.''
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2 May 2024: CBDs I to X... A major milestone! CBM families 1 to 10 are now complete! These are the old CBD (cellulose-binding domain) families, which used to have roman numerals as part of their nomenclature. A special thank you to all the authors and responsible curators who have contributed to this major milestone. Go have a peek at each of these old school families on their respective CAZypedia pages: CBM1, CBM2, CBM3, CBM4, CBM5, CBM6, CBM7, CBM8, CBM9, and CBM10.
11 February 2024: A "BLAST" from the past, with a fresh update. Author Eduardo Moreno Prieto composed a new page on Glycoside Hydrolase Family 119,a family of bacterial amylases, which was Curator Approved by Stefan Janecek and Bernard Henrissat today. The first member of GH119 was characterized in 2006, and through sequence analysis with GH57 members, Janeček and Kuchtová predicted the active-site residues in 2012. Over a decade later, Eduardo, Bernard, and colleagues finally provided critical experimental support for these predictions. Learn more about this history, and especially the relationship between GH119 and GH57, in CAZypedia.
3 February 2024: A new family of beta-1,2-glucan-cyclizing enzymes. A page on the (currently) newest GH family, Glycoside Hydrolase Family 189, was completed today by Authors Tomoko Masaike, Masahiro Nakajima, and Nobukiyo Tanaka (Masahiro Nakajima is the Responsible Curator). GH189 is a family of bacterial transglycosylases that comprise a critical domain in cyclic beta-1,2-glucan synthase (CGS), because this domain is responsible for the final cyclization step during the biosynthesis of these key effector molecules. The discovery of GH189 builds on similarly exciting work by these authors and their colleagues on beta-1,2-glucan hydrolases in GH144 and GH162, which share a common protein fold with GH189, but have distinct mechansims. Check out the GH189, GH144, and GH162 pages to learn more about this breakthrough work on beta-1,2-glucan-active enzymes!